Detail Information for IndEnz0002018499
IED ID IndEnz0002018499
Enzyme Type ID protease018499
Protein Name Glucosylglycerol-phosphate synthase
EC 2.4.1.213
Glucosyl-glycerol-phosphate synthase
GG-phosphate synthase
GGPS
Gene Name ggpS sll1566
Organism Synechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Merismopediaceae Synechocystis unclassified Synechocystis Synechocystis sp. PCC 6803 Synechocystis sp. (strain PCC 6803 / Kazusa)
Enzyme Sequence MNSSLVILYHREPYDEVRENGKTVYREKKSPNGILPTLKSFFADAEQSTWVAWKQVSPKQKDDFQADMSIEGLGDRCTVRRVPLTAEQVKNFYHITSKEAFWPILHSFPWQFTYDSSDWDNFQHINRLFAEAACADADDNALFWVHDYNLWLAPLYIRQLKPNAKIAFFHHTPFPSVDIFNILPWREAIVESLLACDLCGFHIPRYVENFVAVARSLKPVEITRRVVVDQAFTPYGTALAEPELTTQLRYGDRLINLDAFPVGTNPANIRAIVAKESVQQKVAEIKQDLGGKRLIVSAGRVDYVKGTKEMLMCYERLLERRPELQGEISLVVPVAKAAEGMRIYRNAQNEIERLAGKINGRFAKLSWTPVMLFTSPLAYEELIALFCAADIAWITPLRDGLNLVAKEYVVAKNGEEGVLILSEFAGCAVELPDAVLTNPYASSRMDESIDQALAMDKDEQKKRMGRMYAAIKRYDVQQWANHLLREAYADVVLGEPPQM
Enzyme Length 499
Uniprot Accession Number P74258
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ADP-alpha-D-glucose + sn-glycerol 3-phosphate = 2-O-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:12881, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:57597, ChEBI:CHEBI:87089, ChEBI:CHEBI:456216; EC=2.4.1.213; Evidence={ECO:0000269|PubMed:9733686};
DNA Binding
EC Number 2.4.1.213
Enzyme Function FUNCTION: Involved in salt tolerance by producing GG-phosphate from ADP-glucose and glycerol-3-phosphate (G3P), an intermediate in the synthesis of the osmolyte glucosylglycerol (GG). {ECO:0000269|PubMed:9733686}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan metabolism; glucosylglycerol biosynthesis.
nucleotide Binding
Features Chain (1)
Keywords Cytoplasm;Glycosyltransferase;Reference proteome;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17116240}.
Modified Residue
Post Translational Modification PTM: Seems to be degraded, at least in vitro, by FtsH2. In an ftsH2 disruption strain inactive GGPS accumulates.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 18000013;
Motif
Gene Encoded By
Mass 56,802
Kinetics
Metal Binding
Rhea ID RHEA:12881
Cross Reference Brenda